| UniProt ID | PCDGB_HUMAN | |
|---|---|---|
| UniProt AC | Q9Y5H2 | |
| Protein Name | Protocadherin gamma-A11 | |
| Gene Name | PCDHGA11 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 935 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein. |
|
| Protein Description | Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.. | |
| Protein Sequence | MANRLQRGDRSRLLLLLCIFLGTLRGFRARQIRYSVPEETEKGSFVGNISKDLGLEPRELAKRGVRIVSRGKTQLFAVNPRSGSLITAGRIDREELCETVSSCFLNMELLVEDTLKIYGVEVEIIDINDNAPSFQEDEVEIKVSEHAIPGARFALPNARDPDVGVNSLQSYQLSPNNYFSLQLRGRTDGAKNPELVLEGSLDREKEAAHLLLLTALDGGDPIRKGAVPIRVVVLDVNDHIPMFTQSVYRVSVPENISSGTRVLMVNATDPDEGINGEVMYSFRNMESKASEIFQLDSQTGEVQVRGSLDFEKYRFYEMEIQGQDGGGLFTTTTMLITVVDVNDNAPEITITSSINSILENSPPGTVIALLNVQDQDSGENGQVSCFIPNHLPFKLEKTYGNYYKLITSRVLDRELVQSYNITLTATDQGSPPLSAETHVWLNVADDNDNPPVFPHSSYSAYIPENNPRGASIFSVTALDPDSKQNALVTYSLTDDTVQGVPLSSYVSINSNTGVLYALQSFDYEQFRDLELRVIARDSGDPPLSSNVSLSLFVLDQNDNAPEILYPALPTDGSTGVELAPRSAEPGYLVTKVVAVDKDSGQNAWLSYRLLKASEPGLFAVGEHTGEVRTARALLDRDALKQSLVVAVQDHGQPPLSATVTLTVAVADSIPEVLADLGSLESLANSETSDLSLYLVVAVAAVSCIFLVFVIVLLALRLWRWHKSRLLQASEGGLAGMPTSHFVGVDGVQAFLQTYSHEVSLIADSQKSHLIFPQPNYGDTLISQESCEKSEPLLIAEDSAIILGKCDPTSNQQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 23 | Phosphorylation | LLCIFLGTLRGFRAR HHHHHHHHHCCHHHH | 18.54 | - | |
| 48 | N-linked_Glycosylation | EKGSFVGNISKDLGL CCCCCCEEHHHCCCC | 30.02 | UniProtKB CARBOHYD | |
| 62 | Acetylation | LEPRELAKRGVRIVS CCHHHHHHCCCEEEE | 63.41 | 20167786 | |
| 69 | Phosphorylation | KRGVRIVSRGKTQLF HCCCEEEECCCEEEE | 32.70 | - | |
| 214 | Phosphorylation | AAHLLLLTALDGGDP HHHHHHHHHHHCCCC | 25.74 | 22817900 | |
| 224 | Malonylation | DGGDPIRKGAVPIRV HCCCCCCCCCCCEEE | 52.52 | 30639696 | |
| 255 | N-linked_Glycosylation | YRVSVPENISSGTRV EEEECCCCCCCCCEE | 33.11 | UniProtKB CARBOHYD | |
| 266 | N-linked_Glycosylation | GTRVLMVNATDPDEG CCEEEEEECCCCCCC | 24.13 | UniProtKB CARBOHYD | |
| 407 | Phosphorylation | GNYYKLITSRVLDRE CCHHHHHHHHHCCHH | 22.40 | 24719451 | |
| 420 | N-linked_Glycosylation | RELVQSYNITLTATD HHHHHHCCEEEEEEC | 26.47 | UniProtKB CARBOHYD | |
| 546 | N-linked_Glycosylation | GDPPLSSNVSLSLFV CCCCCCCCEEEEEEE | 24.83 | UniProtKB CARBOHYD | |
| 629 | Phosphorylation | EHTGEVRTARALLDR CCCCCHHHHHHHHCH | 26.18 | 20068231 | |
| 728 | Ubiquitination | HKSRLLQASEGGLAG HHHHHHHHCCCCCCC | 14.98 | 32142685 | |
| 732 | Ubiquitination | LLQASEGGLAGMPTS HHHHCCCCCCCCCCH | 14.33 | 32142685 | |
| 741 | Ubiquitination | AGMPTSHFVGVDGVQ CCCCCHHCCCCCHHH | 5.25 | 32142685 | |
| 754 | Phosphorylation | VQAFLQTYSHEVSLI HHHHHHHHCCEEEEE | 8.62 | 25884760 | |
| 782 | Phosphorylation | NYGDTLISQESCEKS CCCCCEECHHHHCCC | 30.89 | 29514088 | |
| 785 | Phosphorylation | DTLISQESCEKSEPL CCEECHHHHCCCCCE | 21.68 | 29514088 | |
| 822 | Phosphorylation | PNTDWRFSQAQRPGT CCCCCCCCCCCCCCC | 18.94 | 25003641 | |
| 882 | Phosphorylation | TMGLSARYGPQFTLQ CCCCCCCCCCCEEEE | 32.64 | 25884760 | |
| 887 | Phosphorylation | ARYGPQFTLQHVPDY CCCCCCEEEEECCCC | 21.91 | 24961811 | |
| 894 | Phosphorylation | TLQHVPDYRQNVYIP EEEECCCCCCCEEEC | 14.18 | 24927040 | |
| 899 | Phosphorylation | PDYRQNVYIPGSNAT CCCCCCEEECCCCCE | 14.67 | 25884760 | |
| 903 | Phosphorylation | QNVYIPGSNATLTNA CCEEECCCCCEECCC | 20.24 | 24719451 | |
| 906 | Phosphorylation | YIPGSNATLTNAAGK EECCCCCEECCCCCC | 38.06 | 27050516 | |
| 913 | Ubiquitination | TLTNAAGKRDGKAPA EECCCCCCCCCCCCC | 42.46 | 32142685 | |
| 917 | Ubiquitination | AAGKRDGKAPAGGNG CCCCCCCCCCCCCCC | 56.33 | 32142685 | |
| 926 | Ubiquitination | PAGGNGNKKKSGKKE CCCCCCCCCCCCCCC | 64.08 | 32142685 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PCDGB_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PCDGB_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PCDGB_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PCDGB_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND MASSSPECTROMETRY. | |